STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
gatBaspartyl/glutamyl-tRNA amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. (489 aa)    
Predicted Functional Partners:
gatA
aspartyl/glutamyl-tRNA amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln).
 0.999
gatC
asparaginyl/glutamyl-tRNA amidotransferase subunit C; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family.
 
 0.999
APC01204.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
 
 0.991
aspS
aspartate--tRNA ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 
 0.988
glnS
glutamine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.961
guaA
Glutamine-hydrolyzing GMP synthase; Catalyzes the synthesis of GMP from XMP.
  
  
 0.894
pheT
phenylalanine--tRNA ligase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.738
APC02193.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.695
xerC
Recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
       0.694
gltX
glutamate--tRNA ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
  
 
 0.662
Your Current Organism:
Polynucleobacter asymbioticus
NCBI taxonomy Id: 576611
Other names: Burkholderiaceae bacterium KF022, Burkholderiaceae bacterium KF023, Burkholderiaceae bacterium KF032, Burkholderiaceae bacterium KF040, Burkholderiaceae bacterium KF041, Burkholderiaceae bacterium KF042, Burkholderiaceae bacterium KF043, Burkholderiaceae bacterium KF046, Burkholderiaceae bacterium KF047, Burkholderiaceae bacterium KF069, Burkholderiaceae bacterium KF071, Burkholderiaceae bacterium KF072, CIP 109841, DSM 18221, P. asymbioticus, Polynucleobacter asymbioticus (Hahn et al. 2009) Hahn et al. 2016, Polynucleobacter necessarius subsp. asymbioticus, Polynucleobacter necessarius subsp. asymbioticus Hahn et al. 2009, Polynucleobacter sp. INAWF005, Polynucleobacter sp. INAWF006, Polynucleobacter sp. INAWF008, Polynucleobacter sp. INAWF009, Polynucleobacter sp. INAWF010, Polynucleobacter sp. INAWF011, Polynucleobacter sp. INAWF012, Polynucleobacter sp. INBF001, Polynucleobacter sp. MWH-Creno-4A3, Polynucleobacter sp. MWH-Creno-4D65, Polynucleobacter sp. MWH-Mekk-C4, Polynucleobacter sp. MWH-Mekk-D4, Polynucleobacter sp. MWH-NZ4W7a, Polynucleobacter sp. MWH-P1sevC1, Polynucleobacter sp. P1-KOL8, Polynucleobacter sp. QLW-P1DMWA-2, Polynucleobacter sp. QLW-P1DNSYA-1, Polynucleobacter sp. QLW-P1DNSYA-2, Polynucleobacter sp. QLW-P1FAT50D-2, Polynucleobacter sp. QLW-P1FMW50A-1, Polynucleobacter sp. QLW-P1FNSY20A-6, Polynucleobacter sp. SHIRF001, Polynucleobacter sp. SHIRF002, Polynucleobacter sp. SHIRF003, Polynucleobacter sp. SHIRF004, Polynucleobacter sp. SHIRF005, Polynucleobacter sp. SHIRF006, Polynucleobacter sp. SHIRF007, Polynucleobacter sp. SHIRF008, Polynucleobacter sp. SHIRF009, Polynucleobacter sp. SHIRF010, Polynucleobacter sp. SHIRF011, Polynucleobacter sp. SHIRF012, Polynucleobacter sp. SHIRF013, Polynucleobacter sp. SHIRF014, Polynucleobacter sp. SHIRF015, Polynucleobacter sp. SHIRF016, Polynucleobacter sp. SHIRF017, Polynucleobacter sp. SHIRF018, Polynucleobacter sp. SHIRF019, Polynucleobacter sp. SUWAF015, Polynucleobacter sp. SUWAF016, Polynucleobacter sp. TEGAF008, Polynucleobacter sp. TEGF001, Polynucleobacter sp. UF003, Polynucleobacter sp. UF009, Polynucleobacter sp. USHIF002, Polynucleobacter sp. USHIF003, Polynucleobacter sp. USHIF004, Polynucleobacter sp. USHIF007, Polynucleobacter sp. USHIF009, Polynucleobacter sp. USHIF010, Polynucleobacter sp. USHIF011, Polynucleobacter sp. USHIF012, beta proteobacterium MWH-HuK1, beta proteobacterium MWH-T1W11, strain QLW-P1DMWA-1
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.